ArticleCurrent microbiology2016
The Detection of Hemin-Binding Proteins in Riemerella anatipestifer CH-1.
Article in Current microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Multiple TonB-dependent transport systems inInfection and immunity · 2026Article
- Deciphering defensive mechanisms inFrontiers in immunology · 2026Review
- Functional characterization of two TolC in the resistance to drugs and metals and in the virulence ofApplied and environmental microbiology · 2023Article
- An Exposed Outer Membrane Hemin-Binding Protein Facilitates Hemin Transport by a TonB-Dependent Receptor in Riemerella anatipestifer.Applied and environmental microbiology · 2021Article
- Comparative genomics and metabolomics analysis of Riemerella anatipestifer strain CH-1 and CH-2.Scientific reports · 2021Article
- Natural Transformation ofFrontiers in microbiology · 2021Article
- Cas1 and Cas2 From the Type II-C CRISPR-Cas System ofFrontiers in cellular and infection microbiology · 2018Article
- Identifying the Genes Responsible for Iron-Limited Condition inBioMed research international · 2017Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Riemerella anatipestifer (R. anatipestifer) is among the most prevalent duck pathogens, causing acute or chronic septicemia characterized by serositis. Riemerella anatipestifer can be grown on blood-enriched media, in vitro, which provides a hemin source essential for the sustainment of R. anatipestifer and activation of hemin-uptake systems. However, the genes associated with hemin uptake cannot be identified exclusively through genome sequence analysis. Here, we show that R. anatipestifer encodes outer-membrane hemin-binding proteins. Hemin-binding proteins were identified in the cytoplasm with apparent molecular mass of ~45/37/33/23/20/13 kDa, and outer membrane with apparent molecular mass of ~90/70/60/50/15 kDa by batch affinity chromatography and hemin-blotting assays. Our results indicate that these proteins are involved in hemin acquisition. Finally, hemin-binding assay further showed that R. anatipestifer can bind hemin and this capability is increased in iron limited medium, indicating the hemin-uptake system of R. anatipestifer was regulated by iron.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.